Skip to main content
Article

Aldehyde Dehydrogenases in Arabidopsis thaliana: Biochemical Requirements, Metabolic Pathways, and Functional Analysis

Naïm StitiInstitute of Molecular Physiology and Biotechnology of Plants, University of Bonn Bonn, GermanyTagnon D. MissihounUniversity of Bonn, Institute of Molecular Plant Physiology and Biotechnology of Plants, University of Bonn, IMBIO, Kirschallee 1, Bonn, D-53115, GermanySimeon O. KotchoniRutgers University, Biology, 315 Penn St, Camden, NJ 08102, New Jersey, United StatesHans‐Hubert KirchUniversity of Bonn, Institute of Molecular Plant Physiology and Biotechnology of Plants, University of Bonn, IMBIO, Kirschallee 1, Bonn, D-53115, GermanyDorothea BartelsUniversity of Bonn, Institute of Molecular Plant Physiology and Biotechnology of Plants, University of Bonn, IMBIO, Kirschallee 1, Bonn, D-53115, Germany
2011en
ABI

Abstract

Aldehyde dehydrogenases (ALDHs) are a family of enzymes which catalyze the oxidation of reactive aldehydes to their corresponding carboxylic acids. Here we summarize molecular genetic and biochemical analyses of selected ArabidopsisALDH genes. Aldehyde molecules are very reactive and are involved in many metabolic processes but when they accumulate in excess they become toxic. Thus activity of aldehyde dehydrogenases is important in regulating the homeostasis of aldehydes. Overexpression of some ALDH genes demonstrated an improved abiotic stress tolerance. Despite the fact that several reports are available describing a role for specific ALDHs, their precise physiological roles are often still unclear. Therefore a number of genetic and biochemical tools have been generated to address the function with an emphasis on stress-related ALDHs. ALDHs exert their functions in different cellular compartments and often in a developmental and tissue specific manner. To investigate substrate specificity, catalytic efficiencies have been determined using a range of substrates varying in carbon chain length and degree of carbon oxidation. Mutational approaches identified amino acid residues critical for coenzyme usage and enzyme activities.

Identifiers

Citations and references

Cited by 20 references